Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.12.2.1 - cytochrome-c3 hydrogenase and Organism(s) Solidesulfovibrio fructosivorans and UniProt Accession P18187

for references in articles please use BRENDA:EC1.12.2.1
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     1 Oxidoreductases
         1.12 Acting on hydrogen as donor
             1.12.2 With a cytochrome as acceptor
                1.12.2.1 cytochrome-c3 hydrogenase
IUBMB Comments
An iron-sulfur protein. Some forms of the enzyme contain nickel ([NiFe]-hydrogenases) and, of these, some contain selenocysteine ([NiFeSe]-hydrogenases). Methylene blue and other acceptors can also be reduced.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Solidesulfovibrio fructosivorans
UNIPROT: P18187
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
Synonyms
[nife] hydrogenase, [nife]-hydrogenase, [fefe] hydrogenase, [fe]-hydrogenase, [fe] hydrogenase, h2ase, fe-only hydrogenase, [nifese] hydrogenase, hydab, [nifese] hase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cytochrome c3 hydrogenase
-
-
-
-
cytochrome c3 reductase
-
-
-
-
cytochrome hydrogenase
-
-
-
-
H2:ferricytochrome c3 oxidoreductase
-
-
-
-
hydrogenase
-
-
-
-
hydrogenase, cytochrome
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
hydrogen:ferricytochrome-c3 oxidoreductase
An iron-sulfur protein. Some forms of the enzyme contain nickel ([NiFe]-hydrogenases) and, of these, some contain selenocysteine ([NiFeSe]-hydrogenases). Methylene blue and other acceptors can also be reduced.
CAS REGISTRY NUMBER
COMMENTARY hide
9027-05-8
-
9079-91-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
show the reaction diagram
Solidesulfovibrio fructosivorans
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Solidesulfovibrio fructosivorans
-
cytochrome c3 is the natural electron acceptor
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome c3
Solidesulfovibrio fructosivorans
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron
Solidesulfovibrio fructosivorans
-
[Ni,Fe] hydrogenase
Nickel
Solidesulfovibrio fructosivorans
-
[Ni,Fe] hydrogenase
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
O2
Solidesulfovibrio fructosivorans
wild-type tends to attract O2 molecules close to the active site
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Solidesulfovibrio fructosivorans
small subunit
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PHNS_SOLFR
Solidesulfovibrio fructosivorans
314
0
33621
Swiss-Prot
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
V74Q
Solidesulfovibrio fructosivorans
while wild-type tends to attract O2 molecules close to the active site, the V74Q mutant favors the localization of O2 about 20 A away from it. In the mutant, the glutamine residue produces an energy barrier height higher than the one found when a valine is present as in wild-type. In the V74Q mutant, the enzyme inhibition by O2 is lowered from both a kinetic and a thermodynamic point of view with respect to the wild-type enzyme
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
De Luca, G.; De Philip, P.; Dermoun, Z.; Rousset, M.; Vermegljo, A.
Reduction of technetium(VII) by Desulfovibrio fructosovorans is mediated by the nickel-iron hydrogenase
Appl. Environ. Microbiol.
67
4583-4587
2001
Solidesulfovibrio fructosivorans
Manually annotated by BRENDA team
Topin, J.; Rousset, M.; Antonczak, S.; Golebiowski, J.
Kinetics and thermodynamics of gas diffusion in a NiFe hydrogenase
Proteins
80
677-682
2012
Solidesulfovibrio fructosivorans (P18187)
Manually annotated by BRENDA team